Base de dados : MEDLINE
Pesquisa : D12.776.422.316 [Categoria DeCS]
Referências encontradas : 11596 [refinar]
Mostrando: 1 .. 10   no formato [Detalhado]

página 1 de 1160 ir para página                         

  1 / 11596 MEDLINE  
              next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29309785
[Au] Autor:Pathak V; Colah R; Ghosh K
[Ad] Endereço:Department of Haematogenetics, National Institute of Immunohaematology (ICMR), KEM Hospital, Parel 400012, Mumbai, India.
[Ti] Título:Plasmodium falciparum malaria skews globin gene expression balance in in-vitro haematopoietic stem cell culture system: Its implications in malaria associated anemia.
[So] Source:Exp Parasitol;185:29-38, 2018 Feb.
[Is] ISSN:1090-2449
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Understanding the pathophysiology and associated host parasite interactions of the malaria infection is the prerequisite for developing effective prevention and treatment strategies. The exact mechanism underlying malaria associated ineffective and dyserythropoiesis is not yet fully understood. Being an important protein, haemoglobin serves as the main amino acid reservoir available to the intra-erythrocytic plasmodium. It is important to check the expression profiling of globin genes which may help us to understand host parasite interactions and its potential contribution to both infection and disease. Here, an in-vitro culture system was used to study the effect of different doses of Plasmodium falciparum on haematopoietic stem cell expansion, differentiation and expression of globin genes. Upon exposure to the different doses of P. falciparum parasites of strains 3D7, Dd2 and RKL9 (intact and lysed form) at different stages of erythroid development, cells demonstrated suppression in growth and differentiation. At almost all stages of erythroid development upon parasite exposure, the γ globin gene was found to be downregulated and the α/ß as well as α/non- α globin mRNA ratios in late stage erythroid cells were found to be reduced (p < .01) compared to the untreated controls. The imbalance in globin chain expression might be considered as one of the factors involved in malaria associated inappropriate erythropoietic responses.
[Mh] Termos MeSH primário: Anemia/etiologia
Regulação da Expressão Gênica/genética
Globinas/genética
Células-Tronco Hematopoéticas/parasitologia
Malária Falciparum/genética
[Mh] Termos MeSH secundário: Anemia/genética
Anemia/metabolismo
Antígenos CD34/sangue
Biomarcadores/metabolismo
Células Cultivadas
Eritrócitos/parasitologia
Eritrócitos/patologia
Células Eritroides/imunologia
Sangue Fetal/citologia
Globinas/metabolismo
Células-Tronco Hematopoéticas/metabolismo
Hemólise
Interações Hospedeiro-Parasita/genética
Seres Humanos
Malária Falciparum/complicações
Reação em Cadeia da Polimerase em Tempo Real
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antigens, CD34); 0 (Biomarkers); 9004-22-2 (Globins)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180214
[Lr] Data última revisão:
180214
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180109
[St] Status:MEDLINE


  2 / 11596 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29216269
[Au] Autor:Fiocchetti M; Cipolletti M; Marino M
[Ad] Endereço:Department of Science, University of Roma Tre, Viale Guglielmo Marconi, Roma, Italy.
[Ti] Título:Compensatory role of Neuroglobin in nervous and non-nervous cancer cells in response to the nutrient deprivation.
[So] Source:PLoS One;12(12):e0189179, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Environmental factors or adverse growth conditions that may reduce cell function or viability are considered stress. The cell ability to sense and respond to environmental stresses determine its function and survival destiny. We recently defined Neuroglobin (NGB), a heme-protein, as a compensatory protein in the 17ß-Estradiol (E2) anti-apoptotic activity and as a sensor of oxidative stress in both neurons and breast cancer cells. Here, the possibility that NGB levels could represent a pivotal regulator of integrated response of cancer cells to stress has been evaluated. Data obtained in neuroblastoma and in breast cancer cell lines evidence that nutrient deprivation significantly up-regulated NGB levels at different time points. However, the analysis of autophagy activation led to exclude any possible role of stress- or E2-induced NGB in the upstream regulation of general autophagy. However, the over-expression of Flag-NGB in ERα stable transfected HEK-293 cells completely affects nutrient deprivation-induced decrease in cell number. In addition, reported results indicate that modulation of the anti-apoptotic Bcl-2 level may play a key role in the protective NGB function against energetic stress. Overall, these data define a role of NGB as compensatory protein in the cell machinery activated in response to stress and as general stress adaptation marker of cancer cells susceptible to oxidative stress, oxygen and, as demonstrated here for the first time, even to nutrient willingness. Despite the lacking of any direct NGB role on autophagic flux activated by energetic stress, NGB upregulation appears functional in delaying stress-related cell death allowing an appropriate cell response and adaptation to the changing extracellular conditions.
[Mh] Termos MeSH primário: Neoplasias da Mama/patologia
Globinas/fisiologia
Proteínas do Tecido Nervoso/fisiologia
Neuroblastoma/patologia
Neurônios/patologia
[Mh] Termos MeSH secundário: Autofagia
Neoplasias da Mama/metabolismo
Linhagem Celular Tumoral
Meios de Cultura
Globinas/metabolismo
Células HEK293
Seres Humanos
Proteínas do Tecido Nervoso/metabolismo
Neuroblastoma/metabolismo
Neurônios/metabolismo
Estresse Oxidativo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Culture Media); 0 (Nerve Tissue Proteins); 0 (neuroglobin); 9004-22-2 (Globins)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171226
[Lr] Data última revisão:
171226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171208
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0189179


  3 / 11596 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28951213
[Au] Autor:Sugitani K; Koriyama Y; Sera M; Arai K; Ogai K; Wakasugi K
[Ad] Endereço:Department of Clinical Laboratory Science, Graduate School of Medical Science, Kanazawa University, 5-11-80 Kodatsuno, Kanazawa, 920-0942, Japan. Electronic address: sugitani@staff.kanazawa-u.ac.jp.
[Ti] Título:A novel function of neuroglobin for neuroregeneration in mice after optic nerve injury.
[So] Source:Biochem Biophys Res Commun;493(3):1254-1259, 2017 Nov 25.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Neuroglobin (Ngb) is a recently discovered heme protein in the vertebrate brain that can bind to oxygen molecules. Mammalian Ngb plays a crucial role in neuroprotection under conditions of oxidative stress. To investigate other potential functions of Ngb, we investigated the mouse retinal Ngb system following optic nerve injury. In the retina of control mice, Ngb immunoreactivity was limited to the retinal ganglion cell (RGC) layer, and this immunoreactivity rapidly decreased to less than 50% of the control level 5 days after optic nerve injury. On the basis of this decrease, we designed in vivo experiments with enhanced expression of Ngb using adult mouse retina. The enhanced expression of Ngb was achieved by injecting chimeric human Ngb protein, which included the cell membrane-penetrating module of fish Ngb. One-day pretreatment with chimeric Ngb increased immunoreactivity levels of Ngb two-fold in mouse RGCs and increased the number of surviving RGCs three-fold by 14 days after optic nerve injury compared with vehicle controls. Furthermore, in the mouse retinas showing enhanced Ngb expression, several regenerating central optic axons exhibited outgrowth and were found to pass through the nerve crush site 14 days after nerve injury. No such regenerating optic axons were observed in the control mouse optic nerve during the same time frame. The data obtained from in vivo experiments strongly indicate that mammalian Ngb has neuroprotective and neuroregenerative properties.
[Mh] Termos MeSH primário: Globinas/metabolismo
Regeneração Nervosa/fisiologia
Proteínas do Tecido Nervoso/metabolismo
Traumatismos do Nervo Óptico/metabolismo
[Mh] Termos MeSH secundário: Animais
Sobrevivência Celular
Seres Humanos
Masculino
Camundongos Endogâmicos C57BL
Regeneração Nervosa/efeitos dos fármacos
Proteínas Recombinantes/administração & dosagem
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Células Ganglionares da Retina/metabolismo
Células Ganglionares da Retina/patologia
Células Ganglionares da Retina/fisiologia
Proteínas de Peixe-Zebra/genética
Proteínas de Peixe-Zebra/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Nerve Tissue Proteins); 0 (Recombinant Proteins); 0 (Zebrafish Proteins); 0 (neuroglobin); 9004-22-2 (Globins)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171027
[Lr] Data última revisão:
171027
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170928
[St] Status:MEDLINE


  4 / 11596 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28918749
[Au] Autor:Wu M; Chen N; Huang CX; He Y; Zhao YZ; Chen XH; Chen XL; Wang HL
[Ad] Endereço:Ministry of Education, Huazhong Agricultural University, College of Fishery, Key Lab of Freshwater Animal Breeding, Key Lab of Agricultural Animal Genetics, Breeding, and Reproduction, Wuhan, 430070, PR China. hbauwhl@hotmail.com.
[Ti] Título:Effect of Low Temperature on Globin Expression, Respiratory Metabolic Enzyme Activities, and Gill Structure of Litopenaeus vannamei.
[So] Source:Biochemistry (Mosc);82(7):844-851, 2017 Jul.
[Is] ISSN:1608-3040
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Low temperature frequently influences growth, development, and even survival of aquatic animals. In the present study, physiological and molecular responses to low temperature in Litopenaeus vannamei were investigated. The cDNA sequences of two oxygen-carrying proteins, cytoglobin (Cygb) and neuroglobin (Ngb), were isolated. Protein structure analysis revealed that both proteins share a globin superfamily domain. Real-time PCR analysis indicated that Cygb and Ngb mRNA levels gradually increased during decrease in temperatures from 25 to 15°C and then decreased at 10°C in muscle, brain, stomach, and heart, except for a continuing increase in gills, whereas they showed a different expression trend in the hepatopancreas. Hemocyanin concentration gradually reduced as the temperature decreased. Moreover, the activities of respiratory metabolic enzymes including lactate dehydrogenase (LDH) and succinate dehydrogenase (SDH) were measured, and it was found that LDH activity gradually increased while SDH activity decreased after low-temperature treatment. Finally, damage to gill structure at low temperature was also observed, and this intensified with further decrease in temperature. Taken together, these results show that low temperature has an adverse influence in L. vannamei, which contributes to systematic understanding of the adaptation mechanisms of shrimp at low temperature.
[Mh] Termos MeSH primário: Temperatura Baixa
Regulação da Expressão Gênica
Globinas/genética
Proteínas do Tecido Nervoso/genética
Penaeidae/anatomia & histologia
Penaeidae/fisiologia
[Mh] Termos MeSH secundário: Animais
Bases de Dados Factuais
Brânquias/anatomia & histologia
Brânquias/metabolismo
Globinas/química
Globinas/metabolismo
Hemocianinas/análise
Hepatopâncreas/metabolismo
L-Lactato Desidrogenase/genética
L-Lactato Desidrogenase/metabolismo
Proteínas do Tecido Nervoso/química
Proteínas do Tecido Nervoso/metabolismo
Penaeidae/enzimologia
Penaeidae/genética
RNA Mensageiro/metabolismo
Reação em Cadeia da Polimerase em Tempo Real
Succinato Desidrogenase/genética
Succinato Desidrogenase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Nerve Tissue Proteins); 0 (RNA, Messenger); 0 (cytoglobin); 0 (neuroglobin); 9004-22-2 (Globins); 9013-72-3 (Hemocyanins); EC 1.1.1.27 (L-Lactate Dehydrogenase); EC 1.3.99.1 (Succinate Dehydrogenase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170919
[St] Status:MEDLINE
[do] DOI:10.1134/S0006297917070100


  5 / 11596 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28899945
[Au] Autor:Wu G; Zhao J; Franzen S; Tsai AL
[Ad] Endereço:Division of Hematology, Department of Internal Medicine, The University of Texas Health Science Center at Houston - McGovern Medical School, Houston, TX 77030, U.S.A.
[Ti] Título:Bindings of NO, CO, and O to multifunctional globin type dehaloperoxidase follow the 'sliding scale rule'.
[So] Source:Biochem J;474(20):3485-3498, 2017 Oct 05.
[Is] ISSN:1470-8728
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Dehaloperoxidase-hemoglobin (DHP), a multifunctional globin protein, not only functions as an oxygen carrier as typical globins such as myoglobin and hemoglobin, but also as a peroxidase, a mono- and dioxygenase, peroxygenase, and an oxidase. Kinetics of DHP binding to NO, CO, and O were characterized for wild-type DHP A and B and the H55D and H55V DHP A mutants using stopped-flow methods. All three gaseous ligands bind to DHP significantly more weakly than sperm whale myoglobin (SWMb). Both CO and NO bind to DHP in a one-step process to form a stable six-coordinate complex. Multiple-step NO binding is not observed in DHP, which is similar to observations in SWMb, but in contrast with many heme sensor proteins. The weak affinity of DHP for O is mainly due to a fast O dissociation rate, in accordance with a longer N-Fe distance between the heme iron and distal histidine in DHP than that in Mb, and an open-distal pocket that permits ligand escape. Binding affinities in DHP show the same 3-4 orders separation between the pairs NO/CO and CO/O , consistent with the 'sliding scale rule' hypothesis. Strong gaseous ligand discrimination by DHP is very different from that observed in typical peroxidases, which show poor gaseous ligand selectivity, correlating with a neutral proximal imidazole ligand rather than an imidazolate. The present study provides useful insights into the rationale for DHP to function both as mono-oxygenase and oxidase, and is the first example of a globin peroxidase shown to follow the 'sliding scale rule' hypothesis in gaseous ligand discrimination.
[Mh] Termos MeSH primário: Monóxido de Carbono/metabolismo
Globinas/metabolismo
Óxido Nítrico/metabolismo
Oxigênio/metabolismo
Peroxidases/metabolismo
[Mh] Termos MeSH secundário: Hemoglobinas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Hemoglobins); 31C4KY9ESH (Nitric Oxide); 7U1EE4V452 (Carbon Monoxide); 9004-22-2 (Globins); EC 1.11.1.- (Peroxidases); S88TT14065 (Oxygen)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171012
[Lr] Data última revisão:
171012
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170914
[St] Status:MEDLINE
[do] DOI:10.1042/BCJ20170515


  6 / 11596 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28798140
[Au] Autor:Jourd'heuil FL; Xu H; Reilly T; McKellar K; El Alaoui C; Steppich J; Liu YF; Zhao W; Ginnan R; Conti D; Lopez-Soler R; Asif A; Keller RK; Schwarz JJ; Thanh Thuy LT; Kawada N; Long X; Singer HA; Jourd'heuil D
[Ad] Endereço:From the Department of Molecular and Cellular Physiology (F.L.J., H.X., T.R., K.M., C.E.A., J.S., Y.F.L., W.Z., R.G., R.K.K., J.J.S., X.L., H.A.S., D.J.) and Surgery Transplantation (D.C., R.L.-S.), Albany Medical Center, NY; Seton Hall-Hackensack Meridian School of Medicine, Jersey Shore University
[Ti] Título:The Hemoglobin Homolog Cytoglobin in Smooth Muscle Inhibits Apoptosis and Regulates Vascular Remodeling.
[So] Source:Arterioscler Thromb Vasc Biol;37(10):1944-1955, 2017 Oct.
[Is] ISSN:1524-4636
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:OBJECTIVE: The role of hemoglobin and myoglobin in the cardiovascular system is well established, yet other globins in this context are poorly characterized. Here, we examined the expression and function of cytoglobin (CYGB) during vascular injury. APPROACH AND RESULTS: We characterized CYGB content in intact vessels and primary vascular smooth muscle (VSM) cells and used 2 different vascular injury models to examine the functional significance of CYGB in vivo. We found that CYGB was strongly expressed in medial arterial VSM and human veins. In vitro and in vivo studies indicated that CYGB was lost after VSM cell dedifferentiation. In the rat balloon angioplasty model, site-targeted delivery of adenovirus encoding shRNA specific for CYGB prevented its reexpression and decreased neointima formation. Similarly, 4 weeks after complete ligation of the left common carotid, knockout mice displayed little to no evidence of neointimal hyperplasia in contrast to their wild-type littermates. Mechanistic studies in the rat indicated that this was primarily associated with increased medial cell loss, terminal uridine nick-end labeling staining, and caspase-3 activation, all indicative of prolonged apoptosis. In vitro, CYGB could be reexpressed after VSM stimulation with cytokines and hypoxia and loss of CYGB sensitized human and rat aortic VSM cells to apoptosis. This was reversed after antioxidant treatment or NOS2 (nitric oxide synthase 2) inhibition. CONCLUSIONS: These results indicate that CYGB is expressed in vessels primarily in differentiated medial VSM cells where it regulates neointima formation and inhibits apoptosis after injury.
[Mh] Termos MeSH primário: Apoptose
Globinas/fisiologia
Músculo Liso Vascular/citologia
Músculo Liso Vascular/fisiopatologia
Remodelação Vascular/fisiologia
[Mh] Termos MeSH secundário: Animais
Caspase 3/metabolismo
Diferenciação Celular
Regulação para Baixo
Ativação Enzimática
Camundongos
Camundongos Knockout
Músculo Liso Vascular/efeitos dos fármacos
Neointima/fisiopatologia
Óxido Nítrico Sintase Tipo II/toxicidade
Oxirredução
Ratos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (cytoglobin); 9004-22-2 (Globins); EC 1.14.13.39 (Nitric Oxide Synthase Type II); EC 3.4.22.- (Caspase 3)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171010
[Lr] Data última revisão:
171010
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170812
[St] Status:MEDLINE
[do] DOI:10.1161/ATVBAHA.117.309410


  7 / 11596 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28792538
[Au] Autor:Wan X; Saito JA; Newhouse JS; Hou S; Alam M
[Ad] Endereço:Department of Microbiology, University of Hawaii, Honolulu, Hawaii, United States of America.
[Ti] Título:The importance of conserved amino acids in heme-based globin-coupled diguanylate cyclases.
[So] Source:PLoS One;12(8):e0182782, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Globin-coupled diguanylate cyclases contain globin, middle, and diguanylate cyclase domains that sense O2 to synthesize c-di-GMP and regulate bacterial motility, biofilm formation, and virulence. However, relatively few studies have extensively examined the roles of individual residues and domains of globin-coupled diguanylate cyclases, which can shed light on their signaling mechanisms and provide drug targets. Here, we report the critical residues of two globin-coupled diguanylate cyclases, EcGReg from Escherichia coli and BpeGReg from Bordetella pertussis, and show that their diguanylate cyclase activity requires an intact globin domain. In the distal heme pocket of the globin domain, residues Phe42, Tyr43, Ala68 (EcGReg)/Ser68 (BpeGReg), and Met69 are required to maintain full diguanylate cyclase activity. The highly conserved amino acids His223/His225 and Lys224/Lys226 in the middle domain of EcGReg/BpeGReg are essential to diguanylate cyclase activity. We also identified sixteen important residues (Leu300, Arg306, Asp333, Phe337, Lys338, Asn341, Asp342, Asp350, Leu353, Asp368, Arg372, Gly374, Gly375, Asp376, Glu377, and Phe378) in the active site and inhibitory site of the diguanylate cyclase domain of EcGReg. Moreover, BpeGReg266 (residues 1-266) and BpeGReg296 (residues 1-296), which only contain the globin and middle domains, can inhibit bacterial motility. Our findings suggest that the distal residues of the globin domain affect diguanylate cyclase activity and that BpeGReg may interact with other c-di-GMP-metabolizing proteins to form mixed signaling teams.
[Mh] Termos MeSH primário: Proteínas de Escherichia coli/genética
Proteínas de Escherichia coli/metabolismo
Globinas/metabolismo
Heme/metabolismo
Fósforo-Oxigênio Liases/genética
Fósforo-Oxigênio Liases/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Bordetella pertussis/enzimologia
Bordetella pertussis/genética
Sequência Conservada
Escherichia coli/enzimologia
Escherichia coli/genética
Modelos Moleculares
Mutação
Fenótipo
Domínios Proteicos
Estrutura Secundária de Proteína
Salmonella typhimurium
Homologia de Sequência de Aminoácidos
Natação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Escherichia coli Proteins); 42VZT0U6YR (Heme); 9004-22-2 (Globins); EC 4.6.- (Phosphorus-Oxygen Lyases); EC 4.6.1.- (diguanylate cyclase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171003
[Lr] Data última revisão:
171003
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170810
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0182782


  8 / 11596 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28671819
[Au] Autor:Amdahl MB; Sparacino-Watkins CE; Corti P; Gladwin MT; Tejero J
[Ad] Endereço:Heart, Lung, Blood, and Vascular Medicine Institute, University of Pittsburgh , Pittsburgh, Pennsylvania 15213, United States.
[Ti] Título:Efficient Reduction of Vertebrate Cytoglobins by the Cytochrome b /Cytochrome b Reductase/NADH System.
[So] Source:Biochemistry;56(30):3993-4004, 2017 Aug 01.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Cytoglobin is a heme-containing protein ubiquitous in mammalian tissues. Unlike the evolutionarily related proteins hemoglobin and myoglobin, cytoglobin shows a six-coordinated heme binding, with the heme iron coordinated by two histidine side chains. Cytoglobin is involved in cytoprotection pathways through yet undefined mechanisms, and it has recently been demonstrated that cytoglobin has redox signaling properties via nitric oxide (NO) and nitrite metabolism. The reduced, ferrous cytoglobin can bind oxygen and will react with NO in a dioxygenation reaction to form nitrate, which dampens NO signaling. When deoxygenated, cytoglobin can bind nitrite and reduce it to NO. This oxidoreductase activity could be catalytic if an effective reduction system exists to regenerate the reduced heme species. The nature of the physiological cytoglobin reducing system is unknown, although it has been proposed that ascorbate and cytochrome b could fulfill this role. Here we describe that physiological concentrations of cytochrome b and cytochrome b reductase can reduce human and fish cytoglobins at rates up to 250-fold higher than those reported for their known physiological substrates, hemoglobin and myoglobin, and up to 100-fold faster than 5 mM ascorbate. These data suggest that the cytochrome b /cytochrome b reductase system is a viable reductant for cytoglobin in vivo, allowing for catalytic oxidoreductase activity.
[Mh] Termos MeSH primário: Citocromo-B(5) Redutase/metabolismo
Citocromos b5/metabolismo
Globinas/metabolismo
Modelos Moleculares
NAD/metabolismo
Óxido Nítrico/metabolismo
Oxigenases/metabolismo
[Mh] Termos MeSH secundário: Animais
Antioxidantes/química
Biocatálise
Simulação por Computador
Citocromo-B(5) Redutase/química
Citocromo-B(5) Redutase/genética
Citocromos b5/química
Citocromos b5/genética
Globinas/química
Globinas/genética
Seres Humanos
Cinética
Proteínas do Tecido Nervoso/química
Proteínas do Tecido Nervoso/genética
Proteínas do Tecido Nervoso/metabolismo
Oxirredução
Oxigenases/química
Oxigenases/genética
Conformação Proteica
Isoformas de Proteínas/química
Isoformas de Proteínas/genética
Isoformas de Proteínas/metabolismo
Proteínas Recombinantes de Fusão/química
Proteínas Recombinantes de Fusão/metabolismo
Proteínas Recombinantes/química
Proteínas Recombinantes/metabolismo
Homologia Estrutural de Proteína
Proteínas de Peixe-Zebra/química
Proteínas de Peixe-Zebra/genética
Proteínas de Peixe-Zebra/metabolismo
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antioxidants); 0 (CYB5A protein, human); 0 (Nerve Tissue Proteins); 0 (Protein Isoforms); 0 (Recombinant Fusion Proteins); 0 (Recombinant Proteins); 0 (Zebrafish Proteins); 0 (cytoglobin); 0 (neuroglobin); 0U46U6E8UK (NAD); 31C4KY9ESH (Nitric Oxide); 9004-22-2 (Globins); 9035-39-6 (Cytochromes b5); EC 1.13.- (Oxygenases); EC 1.14.13.- (nitric oxide dioxygenase); EC 1.6.2.2 (CYB5R3 protein, human); EC 1.6.2.2 (Cytochrome-B(5) Reductase)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170815
[Lr] Data última revisão:
170815
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170704
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.7b00224


  9 / 11596 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28662027
[Au] Autor:Cai G; Chen B; Li Z; Wei W; Wang P; Dong W
[Ad] Endereço:Department of Laboratory Medicine and Biotechnology, Southern Medical University, Guangzhou, Guangdong Province, PR China.
[Ti] Título:The different expressed serum proteins in rhCygb treated rat model of liver fibrosis by the optimized two-dimensional gel electrophoresis.
[So] Source:PLoS One;12(6):e0177968, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Liver fibrosis, a common pathological process of chronic liver diseases, is the final stage of liver dysfunction that has severely deleterious impact on human health. Cytoglobin was first discovered in 2001 by proteomic analysis in rat stellate cells and was reported to play an important role in controlling tissue fibrosis. However, the mechanism by which cytoglobin inhibits or reverses the progression of fibrosis remains unclear. The present study examines the effect of recombinant human cytoblobin (rhCygb) in a rat model of liver fibrosis. Proteomic approaches were employed to identify differentially expressed proteins in the fibrosis model. Optimized conditions for two-dimensional gel electrophoresis were developed to provide improved protein detection and separation. A total of 43 spots were obtained and, through the use of matrix-assisted laser desorption ionization time-of-flight mass spectrometry, 30 differentially expressed proteins were identified. Gene ontology term annotation and KEGG pathway analysis allowed us to explore the function of the represented proteins. Based on these results, we provide a theory of the molecular mechanism related to rhCygb reversion of fibrosis and which will assist in the identification of biomarkers in patient serum to improve early diagnosis of liver fibrosis.
[Mh] Termos MeSH primário: Proteínas Sanguíneas/metabolismo
Modelos Animais de Doenças
Eletroforese em Gel Bidimensional/métodos
Globinas/administração & dosagem
Cirrose Hepática/metabolismo
[Mh] Termos MeSH secundário: Animais
Masculino
Ratos
Ratos Sprague-Dawley
Proteínas Recombinantes/administração & dosagem
Espectrometria de Massas por Ionização e Dessorção a Laser Assistida por Matriz
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Blood Proteins); 0 (Recombinant Proteins); 0 (cytoglobin); 9004-22-2 (Globins)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170928
[Lr] Data última revisão:
170928
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170630
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0177968


  10 / 11596 MEDLINE  
              first record previous record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28447426
[Au] Autor:Clark BE; Shooter C; Smith F; Brawand D; Thein SL
[Ad] Endereço:Department of Molecular Pathology, Viapath at King's College Hospital NHS Foundation Trust, London, UK.
[Ti] Título:Next-generation sequencing as a tool for breakpoint analysis in rearrangements of the globin gene clusters.
[So] Source:Int J Lab Hematol;39 Suppl 1:111-120, 2017 May.
[Is] ISSN:1751-553X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:INTRODUCTION: Next-generation sequencing (NGS), now embedded within genomic laboratories, is well suited to the detection of small sequence changes but is less well adapt for detecting structural variants (SV), mainly due to the relatively short sequence reads. Of the available target enrichment methods, bait capture or whole-genome sequencing appears better suited to detecting SV as there is less PCR amplification and is therefore more representative of the genome being sequenced. MATERIAL AND METHODS: In 2015, we described the first inversion/deletion causing εγδß- thalassemia using an NGS approach, with base-pair resolution. Bioinformatic processing of the sequencing data was manual and time-consuming. The methodology relied on detecting the presence or absence of the SV by assessing sequence coverage and then mapping the deletion by capturing and sequencing breakpoint spanning reads (split reads). In the period between developing more automated analytical methods, we identified the first duplication of the entire beta globin cluster. RESULTS: Detecting the presence of the SV is reliable but capturing the breakpoint spanning reads is challenging. Confirmation by Sanger sequencing a breakpoint spanning amplicon has confirmed the NGS results in all cases. CONCLUSIONS: We have now streamlined and automated the bioinformatic approach using Exome Depth to assess sequence coverage and Delly to detect split and discordant reads. The combined NGS and bioinformatic strategy has proven to be highly successful and applicable to routine diagnostics.
[Mh] Termos MeSH primário: Pontos de Quebra do Cromossomo
Rearranjo Gênico
Genoma Humano
Globinas/genética
Sequenciamento de Nucleotídeos em Larga Escala/métodos
Família Multigênica
Talassemia/genética
[Mh] Termos MeSH secundário: Seres Humanos
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
9004-22-2 (Globins)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170612
[Lr] Data última revisão:
170612
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170428
[St] Status:MEDLINE
[do] DOI:10.1111/ijlh.12680



página 1 de 1160 ir para página                         
   


Refinar a pesquisa
  Base de dados : MEDLINE Formulário avançado   

    Pesquisar no campo  
1  
2
3
 
           



Search engine: iAH v2.6 powered by WWWISIS

BIREME/OPAS/OMS - Centro Latino-Americano e do Caribe de Informação em Ciências da Saúde